CTTB2_MUSPF
ID CTTB2_MUSPF Reviewed; 1645 AA.
AC Q07E15;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Cortactin-binding protein 2;
DE Short=CortBP2;
GN Name=CTTNBP2; Synonyms=CORTBP2;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Mustela.
OX NCBI_TaxID=9669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates the dendritic spine distribution of CTTN/cortactin
CC in hippocampal neurons, thus controls dendritic spinogenesis and
CC dendritic spine maintenance. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTTN/cortactin SH3 domain. Interacts with STRN,
CC STRN4/zinedin and MOB4/phocein; this interaction may regulate dendritic
CC spine distribution of STRN and STRN4 in hippocampal neurons. Activation
CC of glutamate receptors weakens the interaction with STRN and STRN4.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cell
CC projection, dendritic spine {ECO:0000250}. Note=Remains associated with
CC dendritic spines even after glutamate stimulation. {ECO:0000250}.
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DR EMBL; DP000183; ABI93661.1; -; Genomic_DNA.
DR RefSeq; XP_004741960.2; XM_004741903.1.
DR AlphaFoldDB; Q07E15; -.
DR SMR; Q07E15; -.
DR STRING; 9668.ENSMPUP00000007067; -.
DR Ensembl; ENSMPUT00000007185; ENSMPUP00000007067; ENSMPUG00000007124.
DR GeneID; 101671972; -.
DR KEGG; mpuf:101671972; -.
DR CTD; 83992; -.
DR eggNOG; ENOG502QWG2; Eukaryota.
DR GeneTree; ENSGT00940000158293; -.
DR HOGENOM; CLU_004926_0_0_1; -.
DR InParanoid; Q07E15; -.
DR OMA; MCPVEAL; -.
DR Proteomes; UP000000715; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IEA:Ensembl.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR019131; Cortactin-binding_p2_N.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF09727; CortBP2; 2.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 3: Inferred from homology;
KW ANK repeat; Cell projection; Coiled coil; Cytoplasm; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1645
FT /note="Cortactin-binding protein 2"
FT /id="PRO_0000260410"
FT REPEAT 706..736
FT /note="ANK 1"
FT REPEAT 740..769
FT /note="ANK 2"
FT REPEAT 773..802
FT /note="ANK 3"
FT REPEAT 806..835
FT /note="ANK 4"
FT REPEAT 839..868
FT /note="ANK 5"
FT REPEAT 909..939
FT /note="ANK 6"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 119..276
FT /evidence="ECO:0000255"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 495
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:B9EJA2"
FT MOD_RES 1521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZ74"
SQ SEQUENCE 1645 AA; 178410 MW; 10FC05FE92A20D44 CRC64;
MATDGASCEP DFSRAPEDAE GATAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGAGEKEK KPVCTNPLSI LEAVMAHCRK
MQERMSTQLA AAESRQKKLE MEKLQLQGLE QEHKQLAARL EEERGKNKHV VLMLVKECKQ
LSGKVLDEAQ KLEDVLARLE EEKKKTGTLE EQLSAEKRKS TEMEAQMEKQ LSEFDTEREQ
LRAKLHREEA HTTDLKEEID KMKKMIEQLK RGNDSKPSLS LPRKTKDRRS VSISVGTEGP
VTRSVACQTD PAVESIDHVK KLPLTVPVKP PTGSPLVSAN TKGNVCPSAA LGRPGIDRQA
SHGDLIVSSL PTVPPPSASK IEENGPSTGS PSSTPPLPNS TAPPTVQTPT IAPQSHAQAA
PGHSLHSPCA NAALHPGLNP RIQAARFRFQ GNANDPDQNG NTTQSPPSRD VSPTSRDSLV
AKQLARNTVT QALSRFTSPP AGAPPRPGAP STGDVGTCPP VGRTSLKTPG VARVDRGNPP
PIPPKKPGLS QTPSPPHPQL KVIMDSSRAS SAGAKVDNKT MASPPSTLPQ GNRVINEENL
PKSSSPQLPP KPSIDLTVAP AGCGVSALAT SQVGAWPAET PGLSQPACSE SSLVIPTTIA
FCSSINPVSA SSCRTGASDS LLVAASGWSP SLTPLLMSGG PAPLAGRPTL LQQAAAQGNV
TLLSMLLNEE GLDINYSCED GHSALYSAAK NGHTDCVRLL LNAEAQVNAA DKNGFTPLCA
AAAQGHFKCV ELLIAYNANI NHAADEGQTP LYLACKNGNK ECIKHLLEAG TDRSVKTRDG
WTPVHAAVDA GNVDSLKLLM YHRAPARRNS LHEEEPESGV FDLDQGEESP EGTSKPVIPA
DLINHADREG WTAAHIAASK GFKDCLEILC KHRGLEPERR DKCNRTAHDV ATDDCKHLLE
NLNALKIPVR ISGGESPPGN YGSDDFECEN TICALNIRKQ TSWEDFSKAV SQALTNHFQA
ISSDGWRSLE DGTFNNTTDS CIGLSTSSVR SVMLGNVPWS TGQSFSQSPW DFMKKNKAEQ
VTVFLSGPQE GCLSSVTYTS MIPLQMLQNY LRLVEQYHNV IFHGPEGSLQ DYVAHQLALC
MKHRQMAAGF TCEIVRAKVD AGFSKEQLGD LFISSACLIP VKQSPMNKKV IIVLENLEKC
SLSELLGDFL APLENRSTES PWILQKGNGT SECYYFHENC FLMGTIAKAC LQGSDLLVQQ
HFRWVQLRWD GEPMQGLLPR FLRRKVMNKF RGQVPSPCDP VCKTVDWALA VWRQLNSCLA
RLGTPEALLG PEYFLSCPVV PGHAQATVKW MAKLWNAVIA PRVQEAVLSR ASVRRQPGLG
LTAARSRPSQ GQQAVVKVAL SILLNKAVLH GCPLQRADLD QHVADFKGGA FPLSIVSSYN
SCSRKKGESG AWRKVSTSPR KKSGRFSPPS WSKPGPSEEG IKVKAISQLN YNRNASLSKQ
KSLENDLSLT LNLEQRLSLG SDDEADLVQE LQSMCSSKSE SDISKIADSR DDLRSFDSPG
NSPAFSATVN PRMPVSPKEV SPFSSHQPTE CSNSQSKMEL GVSRVKSFLP VPRSKVTQCS
QNTKRSSSSS NTRQIEINNN SKEEI
